enzyme Name NADPH hemoprotein reductase EC number 1.6.2.4 CAS number 9023 03 4 IUBMB EC number 1 6 2 4 GO code 0003958 image width caption In enzymology , a NADPH hemoprotein reductase EC number 1.6.2.4 is an enzyme that catalysis catalyzes the chemical reaction NADPH H sup sup n oxidized hemoprotein math rightleftharpoons math NADP sup sup n reduced hemoprotein The 3 substrate biochemistry substrates of this enzyme are nicotinamide adenine dinucleotide phosphate NADPH , hydrogen ion H sup sup , and oxidized hemoprotein , whereas its two product chemistry products are nicotinamide adenine dinucleotide phosphate NADP sup sup and reduced hemoprotein . This enzyme belongs to the family of oxidoreductase s, specifically those acting on NADH or NADPH with a heme protein as acceptor. The systematic name of this enzyme class is NADPH hemoprotein oxidoreductase . Other names in common use include CPR , FAD cytochrome c reductase , NADP cytochrome c reductase , NADP cytochrome reductase , NADPH dependent cytochrome c reductase , NADPH P 450 reductase , NADPH ferrihemoprotein oxidoreductase , NADPH cytochrome P 450 oxidoreductase , NADPH cytochrome c oxidoreductase , NADPH cytochrome c reductase , NADPH cytochrome p 450 reductase , NADPH ferricytochrome c oxidoreductase , NADPH ferrihemoprotein reductase , TPNH2 cytochrome c reductase , TPNH cytochrome c reductase , aldehyde reductase NADPH dependent , cytochrome P 450 reductase , cytochrome c reductase reduced nicotinamide adenine dinucleotide , phosphate, NADPH, NADPH dependent , dihydroxynicotinamide adenine dinucleotide phosphate cytochrome c , reductase , ferrihemoprotein P 450 reductase , reduced nicotinamide adenine dinucleotide phosphate cytochrome c , reductase , reductase, cytochrome c reduced nicotinamide adenine dinucleotide , and phosphate . It has 2 cofactor biochemistry cofactors FAD , and FMN . Structural studies As of late 2007, 10 tertiary structure structures have been solved for this class of enzymes, with Protein ... more details
Image Haem B 3D vdW.png thumb right 200px A space filling model model of Heme B cofactor. A hemeprotein or hemoprotein or haemoprotein , or heme protein , is a metalloprotein containing a heme prosthetic group , either Covalent bond covalently or noncovalently chemical bond bound to the protein itself. The iron in the heme is capable of undergoing oxidation and redox reduction usually to 2 and 3, though stabilized ferryl Fe sup 4 sup and even Fe sup 5 sup species are well known in the peroxidases . Hemoproteins probably evolved from a primordial strategy allowing to incorporate the iron Fe atom contained within the protoporphyrin IX ring of heme into proteins. This strategy has been maintained throughout evolution as it makes hemoproteins responsive to molecules that can bind divalent iron Fe . These molecules included, but are probably not restricted to, gaseous molecules, such as oxygen O sub 2 sub nitric oxide NO , carbon monoxide CO and hydrogen sulfide H sub 2 sub S . Once bound to the prosthetic heme groups of hemoproteins these gaseous molecules can modulate the activity function of those hemoproteins in a way that is said to afford signal transduction. Therefore, when produced in biologic systems cells , these gaseous molecules are referred to as gasotransmitters . Roles Hemoproteins have diverse biological functions including Oxygen transport hemoglobin myoglobin neuroglobin cytoglobin leghemoglobin Catalysis peroxidase s cytochrome c oxidase ligninase s Active transport Active membrane transport cytochrome s Electron transfer cytochrome c catalase Sensory FixL Oxygen sensor sGC Nitric Oxide sensor CooA CO sensor Defence vanabin External links MeshName Hemeproteins Category Hemoproteins protein stub Globins es Hemoprote na fr H moprot ine it Emoproteina ru sv Hemoprotein ... more details
Unreferenced date April 2009 A conjugated protein is a protein that functions in interaction with other chemical groups attached by covalent bond s or by weak interactions. Many proteins contain only amino acid s and no other chemical groups, and they are called simple proteins. However, other kind of proteins yield, on hydrolysis, some other chemical component in addition to amino acids and they are called conjugated proteins. The nonamino part of a conjugated protein is usually called its prosthetic group . Most prosthetic groups are formed from vitamins. Conjugated proteins are classified on the basis of the chemical nature of their prosthetic groups. Some examples of conjugated proteins are lipoprotein s, glycoprotein s, phosphoprotein s, hemoprotein s, flavoprotein s, metalloprotein s, phytochrome s, cytochrome s and opsin s. Haemoglobin contains the prosthetic group containing iron, which is the haem. It is with in the haem group that carries the oxygen molecule through the binding of the oxygen molecule to the iron ion Fe2 found in the haem group. Glycoproteins are generally the largest and most abundant group of conjugated proteins. They range from glycoproteins in cell surface membranes that constitute the glycocalyx , to important antibodies produced by leukocytes . Category Proteins protein stub es Prote na conjugada fr H t roprot ine ja pt Prote na conjugada ru uk zh ... more details
enzyme Name prostaglandin I synthase EC number 5.3.99.4 CAS number 65802 86 0 IUBMB EC number 5 3 99 4 GO code 0008116 image width caption In enzymology , a prostaglandin I synthase EC number 5.3.99.4 is an enzyme that catalysis catalyzes the chemical reaction 5Z,13E 15S 9alpha,11alpha epidioxy 15 hydroxyprosta 5,13 dienoate math rightleftharpoons math 5Z,13E 15S 6,9alpha epoxy 11alpha,15 dihydroxyprosta 5,13 dienoate Thus, the two substrate biochemistry substrates of this enzyme are 5Z,13E 15S 9alpha,11alpha epidioxy 15 hydroxyprosta 5,13 and dienoate , whereas its two product chemistry products are 5Z,13E 15S 6,9alpha epoxy 11alpha,15 dihydroxyprosta 5,13 and dienoate . This enzyme belongs to the family of isomerase s, specifically a class of other intramolecular oxidoreductase s. The systematic name of this enzyme class is 5Z,13E 15S 9alpha,11alpha epidioxy 15 hydroxyprosta 5,13 dienoat e 6 isomerase . Other names in common use include prostacyclin synthase , prostacycline synthetase , prostagladin I2 synthetase , PGI2 synthase , and PGI2 synthetase . This enzyme participates in arachidonic acid metabolism . It employs one cofactor biochemistry cofactor , heme . Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 2IAG . References reflist 1 cite journal author DeWitt DL, Smith WL date 1983 title Purification of prostacyclin synthase from bovine aorta by immunoaffinity chromatography. Evidence that the enzyme is a hemoprotein journal J. Biol. Chem. volume 258 pages 3285&ndash 93 pmid 6338016 issue 5 cite journal author Ullrich V, Castle L, Weber P date 1981 title Spectral evidence for the cytochrome P450 nature of prostacyclin synthetase journal Biochem. Pharmacol. volume 30 pages 2033&ndash 6 pmid 7023490 doi 10.1016 0006 2952 81 90218 5 issue 14 isomerase stub Category EC 5.3.99 Category Heme enzymes Category Enzymes of known structure ... more details
Commented out because image was deleted Image Denis Rousseau.gif thumb Denis L. Rousseau Denis L. Rousseau signing papers as D. L. Rousseau born in New Hampshire, United States U.S. is an United States American scientist . He is currently Professor and University Chairman of the department of Physiology and Biophysics at Albert Einstein College of Medicine . http www.aecom.yu.edu home biophysics Biography Rousseau is professor and University Chairman of Physiology and Biophysics at the Albert Einstein College of Medicine , of Yeshiva University , a position he has held since 1996. He received his B.A. from Bowdoin College and received his Ph. D. in Physical Chemistry from Princeton University . After holding a position as research associate in the Physics Department at the University of Southern California , studying with Sergio Porto , he joined Bell labs AT&T Bell Laboratories in 1969. Research In the 1970s, he used infrared spectroscopy to demonstrate that what was thought to be a newly discovered form of water, polywater , was structurally similar to human sweat. This result suggested that the novel properties of polywater were due to contamination from biological impurities, and later described the proposal of polywater as an example of Pathological science . He is also a pioneer in using Resonance Raman spectroscopy to study hemoprotein heme proteins , notably hemoglobin , Cytochrome c oxidase , Nitric oxide synthase , and the Protein folding folding of cytochrome c . Significant publications cite journal author Rousseau, Denis L. title Case Studies in Pathological Science journal American Scientist year 1992 month January February volume 80 pages 54 63 External links http www.aecom.yu.edu home biophysics rousseau Rousseau Laboratory Persondata Metadata see Wikipedia Persondata . NAME Rousseau, Denis ALTERNATIVE NAMES SHORT DESCRIPTION DATE OF BIRTH PLACE OF BIRTH DATE OF DEATH PLACE OF DEATH DEFAULTSORT Rousseau, Denis Category Bowdoin College alumni Category ... more details
enzyme Name tryptophan 2 dioxygenase EC number 1.13.99.3 CAS number 64295 81 4 IUBMB EC number 1 13 99 3 GO code 0050360 image width caption In enzymology , a tryptophan 2 dioxygenase EC number 1.13.99.3 is an enzyme that catalysis catalyzes the chemical reaction L tryptophan O sub 2 sub math rightleftharpoons math indol 3 yl glycolaldehyde CO sub 2 sub NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are L tryptophan and oxygen O sub 2 sub , whereas its 3 product chemistry products are indol 3 yl glycolaldehyde , carbon dioxide CO sub 2 sub , and ammonia NH sub 3 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on single donors with O sub 2 sub as oxidant and incorporation of two atoms of oxygen into the substrate oxygenases . The oxygen incorporated need not be derived from O miscellaneous. The systematic name of this enzyme class is L tryptophan oxygen 2 oxidoreductase side chain cleaving . Other names in common use include indole 3 alkane alpha hydroxylase , tryptophan side chain alpha,beta oxidase , tryptophan side chain oxidase II , tryptophan side chain oxidase , TSO , indolyl 3 alkan alpha hydroxylase , tryptophan side chain oxidase type I , TSO I , TSO II , and tryptophan side chain oxidase . This enzyme participates in tryptophan metabolism . It employs one cofactor biochemistry cofactor , heme . References reflist 1 cite journal author Roberts J, Rosenfeld HJ date 1977 title Isolation, crystallization, and properties of indolyl 3 alkane alpha hydroxylase. A novel tryptophan metabolizing enzyme journal J. Biol. Chem. volume 252 pages 2640&ndash 7 pmid 15994 issue 8 cite journal author Takai K, Ushiro H, Noda Y, Narumiya S, Tokuyama T date 1977 title Crystalline hemoprotein from Pseudomonas that catalyzes oxidation of side chain of tryptophan and other indole derivatives journal J. Biol. Chem. volume 252 pages 2648&ndash 56 pmid 15995 issue 8 1.13 enzyme stub Category EC 1.13.99 Category Heme ... more details
Orphan date February 2009 Nitrophorins are hemoprotein s found in saliva of Hematophagy blood feeding insects. Saliva of the blood sucking bug Rhodnius prolixus contains at least seven homologous nitrophorins, designated NP1 to NP7 in order of their relative abundance in the glands. As isolated, nitrophorins contain nitric oxide NO ligated to the ferric heme iron Fe sup 3 sup . Histamine , which is released by the host biology host in response to tissue damage, is another nitrophorin ligand. Nitrophorins transport NO to the feeding site. Dilution, binding of histamine and increase in pH from pH 5 in salivary gland to pH 7.4 in the host tissue facilitate the release of NO into the tissue where it induces vasodilator vasodilatation . The salivary nitrophorin from the hemiptera n Cimex lectularius bedbug has no sequence similarity to Rhodnius prolixus nitrophorins but is homologous to the inositol polyphosphate 5 phosphatase EC number 3.1.3.56 . It is suggested that the two classes of insect nitrophorins have arisen as a product of the convergent evolution . The crystal structures of several nitrophorin complexes are known. The Rhodnius prolixus nitrophorin structures reveal lipocalin like eight stranded barrel, three helices and two disulfide bonds, with heme inserted into one end of the barrel. Members of the http scop.mrc lmb.cam.ac.uk scop search.cgi?key lipocalins lipocalin family are known to bind a variety of small hydrophobic ligands, including biliverdin , in a similar fashion. The heme iron is ligated to histidine residue His 59 . The position of His 59 is restrained through water mediated hydrogen bond to the carboxylate of aspartic acid residue Asp 70 . The His 59&ndash Fe bond is bent 15 out of the imidazole plane. Asp 70 forms an unusual hydrogen bond with one of the heme propionates, suggesting the residue has an altered acid dissociation constant p K sub a sub . In NP1 histamine structure, the planes of His 59 and histamine imidazole rings lie in an arrangement ... more details
Image Cytochrome c.png thumb 250px Cytochrome c with heme c . Cytochromes are, in general, membrane bound hemoprotein s that contain heme groups and carry out electron transport . They are found either as Protein subunit monomeric protein s e.g., cytochrome c or as Protein subunit subunits of bigger enzymatic complexes that catalyze redox reactions. They are found in the mitochondrion mitochondrial inner membrane and endoplasmic reticulum of eukaryote s, in the chloroplast s of plants, in photosynthesis photosynthetic microorganism s, and in bacteria . History Cytochromes were initially described in 1884 by MacMunn as respiratory pigments myohematin or histohematin . ref name MacMunn cite journal doi 10.1098 rstl.1886.0007 url http www.jstor.org pss 109482 pages 267 298 author1 Mac Munn, C. A issue 0 title Researches on Myohaematin and the Histohaematins journal Philosophical Transactions of the Royal Society of London volume 177 publisher The Royal Society year 1886 ref In the 1920s, Keilin rediscovered these respiratory pigments and named them the cytochromes, or cellular pigments , and classified these heme proteins, on the basis of the position of their lowest energy absorption band in the reduced state, as cytochromes a 605 nm , b 565 nm , and c 550 nm . The UV visible spectroscopic signatures of hemes are still used to identify heme type from the reduced bis pyridine ligated state, i.e., the pyridine hemochrome method. Within each class, cytochrome a , b , or c , early cytochromes are numbered consecutively, e.g. cyt c , cyt c sub 1 sub , and cyt c sub 2 sub , with more recent examples designated by their reduced state R band maximum, e.g. cyt c sub 559 sub . ref name pmid14871137 cite journal author Reedy, C. J. & Gibney, B. R. title Heme protein assemblies journal Chem Rev volume 104 issue 2 pages 617 49 year 2004 month February pmid 14871137 doi 10.1021 cr0206115 url ref Structure and function The heme group is a highly conjugated ring system ... more details
Leghemoglobin also leghaemoglobin or legoglobin is an nitrogen or oxygen carrier, because naturally occurring oxygen and nitrogen look the same to this protein and a hemoprotein found in the Nitrogen fixation nitrogen fixing root nodules of legume leguminous plants. But nitrogen is need for the cycle to occur. It is produced by legumes in response to the roots being infected by nitrogen fixing bacteria, called rhizobia , as part of the symbiosis symbiotic interaction between plant and bacterium roots uninfected with Rhizobium do not synthesise leghemoglobin. Leghemoglobin has close chemical and structural similarities to hemoglobin , and, like hemoglobin, is red in colour. The protein was believed to be a product of both plant and the bacterium in which the apoprotein is produced by the plant and the heme an iron atom bound in a porphyrin ring is produced by the bacterium . ref cite journal author O Brian, M. R., Kirshbom, P. M., & Maier, R. J. title Bacterial heme synthesis is required for expression of the leghemoglobin holoprotein but not the apoprotein in soybean root nodules journal Proc. Nat. Acad. Sci. USA volume 84 issue 23 pages 8390&ndash 8393 year 1987 url http www.pnas.org content 84 23 8390 doi 10.1073 pnas.84.23.8390 pmid 3479799 pmc 299548 ref Newer findings however, indicate that the heme moiety is also produced by the plant. ref cite journal author Santana, M. A., Pihakaski Maunsbach, K., Sandal, N., Marcker, K. A., & Smith, A. G. title Evidence that the plant host synthesizes the heme moiety of leghemoglobin in root nodules journal Plant Physiol. volume 116 issue 4 pages 1259&ndash 1269 year 1998 url http www.plantphysiol.org cgi content full 116 4 1259 doi 10.1104 pp.116.4.1259 pmid 9536042 pmc 35032 ref In plants infected with Rhizobium , such as alfalfa or soybean s , the presence of oxygen in the root nodules would reduce the activity of the oxygen sensitive nitrogenase an enzyme responsible for the fixation of atmospheric nitrogen. Leghemoglob ... more details
chembox verifiedrevid 413285949 ImageFile 7 nitroindazole.png ImageSize 150 IUPACName 7 nitro 1H indazole OtherNames Section1 Chembox Identifiers InChI 1 C7H5N3O2 c11 10 12 6 3 1 2 5 4 8 9 7 5 6 h1 4H, H,8,9 InChIKey PQCAUHUKTBHUSA UHFFFAOYAE ChEMBL Ref ebicite correct EBI ChEMBL 247378 StdInChI Ref stdinchicite correct chemspider StdInChI 1S C7H5N3O2 c11 10 12 6 3 1 2 5 4 8 9 7 5 6 h1 4H, H,8,9 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey PQCAUHUKTBHUSA UHFFFAOYSA N CASNo 2942 42 9 PubChem 1893 ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 1821 SMILES O N O c1cccc2c1nnc2 Section2 Chembox Properties Formula C sub 7 sub H sub 5 sub N sub 3 sub O sub 2 sub MolarMass 163.1335 Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition 7 Nitroindazole , or 7 NI , is a heterocyclic compound heterocyclic small molecule containing an indazole ring that has been nitration nitrated at the 7 position. Nitroindazole acts as a selective inhibitor for neuron al nitric oxide synthase , a hemoprotein enzyme that, in neuron al tissue, converts arginine to citrulline and nitric oxide NO . ref name Southan cite journal author Southan GJ, Szab C title Selective pharmacological inhibition of distinct nitric oxide synthase isoforms journal Biochem. Pharmacol. volume 51 issue 4 pages 383 94 year 1996 month February pmid 8619882 doi 10.1016 0006 2952 95 02099 3 ref Nitric oxide can diffuse through the plasma membrane into neighbouring cells, allowing cell signalling , so nitroindazole indirectly inhibits this signalling process. ref name pmid7693278 cite journal author Moore PK, Wallace P, Gaffen Z, Hart SL, Babbedge RC title Characterization of the novel nitric oxide synthase inhibitor 7 nitro indazole and related indazoles antinociceptive and cardiovascular effects journal Br. J. Pharmacol. volume 110 issue 1 pages 219 24 year 1993 month September pmid 7693278 doi url issn pmc 2175981 ref ref name pmid7693 ... more details
PBB geneid 1528 Cytochrome b5, form A gene name CYB5A , is a human microsomal cytochrome b5 . ref cite web title Entrez Gene CYB5A Cytochrome b5, form A url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 1528 accessdate ref Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenase s. It has two Protein isoform isoform s produced by alternative splicing . Isoform 1 is bound to the cytoplasmic side of the endoplasmic reticulum . It has a C terminal transmembrane alpha helix. Isoform 2 was found in cytoplasm. Defects in CYB5A are the cause of type IV hereditary methemoglobinemia . References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Ng S, Smith MB, Smith HT, Millett F title Effect of modification of individual cytochrome c lysines on the reaction with cytochrome b5. journal Biochemistry volume 16 issue 23 pages 4975 8 year 1977 pmid 199233 doi 10.1021 bi00642a006 cite journal author Dailey HA, Strittmatter P title Modification and identification of cytochrome b5 carboxyl groups involved in protein protein interaction with cytochrome b5 reductase. journal J. Biol. Chem. volume 254 issue 12 pages 5388 96 year 1979 pmid 221468 doi cite journal author Mitoma J, Ito A title The carboxy terminal 10 amino acid residues of cytochrome b5 are necessary for its targeting to the endoplasmic reticulum. journal EMBO J. volume 11 issue 11 pages 4197 203 year 1992 pmid 1396600 doi pmc 556930 cite journal author Giordano SJ, Steggles AW title The human liver and reticulocyte cytochrome b5 mRNAs are products from a single gene. journal Biochem. Biophys. Res. Commun. volume 178 issue 1 pages 38 44 year 1991 pmid 1712589 doi 10.1016 0006 291X 91 91776 9 cite journal author Shephard EA, Povey S, Spurr NK, Phillips IR title Chromosomal localization of a cytochrome b5 gene to human chromosome 18 and a cytochrome b5 pseudogene to the X chromosome. journal G ... more details
Image Porphyrin.svg thumb right 200px Structure of porphine, the simplest porphyrin Image Heme.svg thumb right 250 px Heme group of hemoglobin. An iron Fe atom in the middle is shown in font color FF0000 red font , complexed to four interior nitrogen atoms shown in font color 0000FF blue font . Porphyrins are a group of organic compound s of which many occur in nature. One of the best known porphyrins is heme , the pigment in red blood cell s heme is a Cofactor biochemistry cofactor of the protein hemoglobin. Porphyrins are heterocyclic macrocycle s composed of four modified pyrrole subunits interconnected at their carbon atoms via methine bridges CH . Porphyrins are aromaticity aromatic . That is, they obey H ckel s rule for aromaticity, possessing 4n 2 electrons n 4 for the shortest cyclic path that are delocalized over the macrocycle. The macrocycles, therefore, are highly conjugated system s. As a consequence, they typically have very intense absorption bands in the visible region and may be deeply colored the name porphyrin comes from a Greek language Greek word for purple . The macrocycle has 26 pi electrons in total. The parent porphyrin is porphine , and substituted porphines are called porphyrins. Complexes of porphyrins and related molecules Porphyrins are the conjugate acids of ligand s that bind metals to form complex chemistry complexes . The metal ion usually has a charge of 2 or 3 . A schematic equation for these syntheses is shown H sub 2 sub porphyrin ML sub n sub sup 2 sup M porphyrinate L sub n 4 sub 4 L 2 H sup sup where M metal ion and L a ligand A porphyrin without metal in its cavity is a free base . Some iron containing porphyrins are called hemes. Heme containing protein s, or hemoprotein s , are found extensively in nature. Hemoglobin and myoglobin are two Oxygen O sub 2 sub binding proteins that contain iron porphyrins. Various cytochrome s are also hemoproteins. Several other heterocycles are related to porphyrins. These include corri ... more details
Image Haem B 3D vdW.png thumb right 200px Space filling model of Heme B Image Heme.png thumb right 200px Ball and Stick model of Heme B A heme American English or haem British English is a prosthetic group that consists of an iron atom contained in the center of a large heterocyclic organic ring called a porphyrin . Not all porphyrins contain iron, but a substantial fraction of porphyrin containing metalloprotein s have heme as their prosthetic group these are known as hemoprotein s. Hemes are most commonly recognized in their presence as components of hemoglobin , the red pigment in blood , but they are also components of a number of other hemoproteins. Function Image Succinate Dehygrogenase 1YQ3 Haem group.png thumb right The histidine bound heme group of succinate dehydrogenase , an electron carrier in the mitochondria l electron transfer chain . The large semi transparent sphere indicates the location of the iron ion . From PDB 1YQ3 . Hemoproteins have diverse biological functions including the transportation of diatomic gases, chemical catalysis , diatomic gas detection, and electron transfer. The heme iron serves as a source or sink of electrons during electron transfer or redox chemistry. In peroxidase reactions, the porphyrin molecule also serves as an electron source. In the transportation or detection of diatomic gases, the gas binds to the heme iron. During the detection of diatomic gases, the binding of the gas ligand to the heme iron induces conformational changes in the surrounding protein. It has been speculated that the original evolutionary function of hemoproteins was electron transfer in primitive sulfur based photosynthesis pathways in ancestral cyanobacteria before the appearance of molecular oxygen. ref cite journal author Hardison, R. title The Evolution of Hemoglobin Studies of a very ancient protein suggest that changes in gene regulation are an important part of the evolutionary story journal American Scientist year 1999 volume 87 issue 2 p ... more details
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